How do Hsp70 chaperones unfold their protein substrates? A novel way to convert chemical energy into mechanical work.
Barducci A., De Los Rios P.
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V - Biofisica e fisica medica
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In this contribution I will describe how Hsp70 chaperones, possibly the most central of all the machines involved in protein quality control in the cell, use the energy liberated by ATP hydrolysis to bind to their substrates and lead to their loss of structure. The mechanism that we unveiled represents a novel addition to the array of force-generating mechanisms in the cell, and is best described as a non-equilibrium steady state, where the action of the chaperone results from a repetitive, continuous binding/unbinding process rather than by a one-shot mechanism.